PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citrate

Abstract Emerging evidence indicates that metabolic signals—including nutrient availability, biosynthetic intermediates, and energy balance—are linked to cell cycle progression. However, how these signals are sensed by the cell cycle machinery remains unclear. Citrate, a key intermediate in the TCA...

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Main Authors: Pianpian Lin, Yijun Qi, Huiying Chu, Hongyu Wu, Yajuan Zhang, Xiaolan Huang, Chen Li, Xiaoyan Xu, Hong Gao, Rong Zeng, Guohui Li, Weiwei Yang
Format: Article
Language:English
Published: Nature Portfolio 2025-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-62111-3
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author Pianpian Lin
Yijun Qi
Huiying Chu
Hongyu Wu
Yajuan Zhang
Xiaolan Huang
Chen Li
Xiaoyan Xu
Hong Gao
Rong Zeng
Guohui Li
Weiwei Yang
author_facet Pianpian Lin
Yijun Qi
Huiying Chu
Hongyu Wu
Yajuan Zhang
Xiaolan Huang
Chen Li
Xiaoyan Xu
Hong Gao
Rong Zeng
Guohui Li
Weiwei Yang
author_sort Pianpian Lin
collection DOAJ
description Abstract Emerging evidence indicates that metabolic signals—including nutrient availability, biosynthetic intermediates, and energy balance—are linked to cell cycle progression. However, how these signals are sensed by the cell cycle machinery remains unclear. Citrate, a key intermediate in the TCA cycle, peaks during mitosis (M phase) and is detected by the glycolytic enzyme ATP-dependent 6-phosphofructokinase 1 muscle isoform (PFKM), accelerating mitotic progression. Mechanistically, citrate binds PFKM, disrupting its tetrameric structure into dimers. Dimeric PFKM interacts with nucleosomes and phosphorylates histone H3 at serine 10 (H3S10), functioning as a protein kinase to promote mitosis and cell proliferation. Structural simulations reveal that PFKM binds nucleosomes optimally when H3S10 aligns with its catalytic site. Disrupting citrate-PFKM or PFKM-H3 interactions reduces H3S10 phosphorylation, delays mitosis, and suppresses tumor growth and T-cell proliferation. Our findings demonstrate that PFKM acts as a citrate sensor, coupling metabolic signals to cell cycle regulation.
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institution Kabale University
issn 2041-1723
language English
publishDate 2025-07-01
publisher Nature Portfolio
record_format Article
series Nature Communications
spelling doaj-art-5e61705bed2e4647a96499dcfc33168d2025-08-20T03:43:00ZengNature PortfolioNature Communications2041-17232025-07-0116112010.1038/s41467-025-62111-3PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citratePianpian Lin0Yijun Qi1Huiying Chu2Hongyu Wu3Yajuan Zhang4Xiaolan Huang5Chen Li6Xiaoyan Xu7Hong Gao8Rong Zeng9Guohui Li10Weiwei Yang11Key Laboratory of Multi-cell Systems, Shanghai Key Laboratory of Molecular Andrology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai Institute of Biochemistry and Cell BiologyKey Laboratory of Systems Health Science of Zhejiang Province, School of Life Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of SciencesInterdisciplinary Research Center for Biology and Chemistry, Liaoning Normal UniversityKey Laboratory of Multi-cell Systems, Shanghai Key Laboratory of Molecular Andrology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai Institute of Biochemistry and Cell BiologyKey Laboratory of Multi-cell Systems, Shanghai Key Laboratory of Molecular Andrology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai Institute of Biochemistry and Cell BiologyKey Laboratory of Systems Health Science of Zhejiang Province, School of Life Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of SciencesCenter for Single-Cell Omics, School of Public Health, Shanghai Jiao Tong University School of MedicineMass Spectrometry & Metabolomics Core Facility, Biomedical Research Core Facilities, Westlake UniversityKey Laboratory of Multi-cell Systems, Shanghai Key Laboratory of Molecular Andrology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai Institute of Biochemistry and Cell BiologyKey Laboratory of Multi-cell Systems, Shanghai Key Laboratory of Molecular Andrology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai Institute of Biochemistry and Cell BiologyInterdisciplinary Research Center for Biology and Chemistry, Liaoning Normal UniversityKey Laboratory of Multi-cell Systems, Shanghai Key Laboratory of Molecular Andrology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai Institute of Biochemistry and Cell BiologyAbstract Emerging evidence indicates that metabolic signals—including nutrient availability, biosynthetic intermediates, and energy balance—are linked to cell cycle progression. However, how these signals are sensed by the cell cycle machinery remains unclear. Citrate, a key intermediate in the TCA cycle, peaks during mitosis (M phase) and is detected by the glycolytic enzyme ATP-dependent 6-phosphofructokinase 1 muscle isoform (PFKM), accelerating mitotic progression. Mechanistically, citrate binds PFKM, disrupting its tetrameric structure into dimers. Dimeric PFKM interacts with nucleosomes and phosphorylates histone H3 at serine 10 (H3S10), functioning as a protein kinase to promote mitosis and cell proliferation. Structural simulations reveal that PFKM binds nucleosomes optimally when H3S10 aligns with its catalytic site. Disrupting citrate-PFKM or PFKM-H3 interactions reduces H3S10 phosphorylation, delays mitosis, and suppresses tumor growth and T-cell proliferation. Our findings demonstrate that PFKM acts as a citrate sensor, coupling metabolic signals to cell cycle regulation.https://doi.org/10.1038/s41467-025-62111-3
spellingShingle Pianpian Lin
Yijun Qi
Huiying Chu
Hongyu Wu
Yajuan Zhang
Xiaolan Huang
Chen Li
Xiaoyan Xu
Hong Gao
Rong Zeng
Guohui Li
Weiwei Yang
PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citrate
Nature Communications
title PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citrate
title_full PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citrate
title_fullStr PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citrate
title_full_unstemmed PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citrate
title_short PFKM phosphorylates histone H3 and promotes mitotic progression by sensing the levels of citrate
title_sort pfkm phosphorylates histone h3 and promotes mitotic progression by sensing the levels of citrate
url https://doi.org/10.1038/s41467-025-62111-3
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